12 by: Ashlynn Jensen
Student: Ashlynn Jensen
Name of enzyme: ATP Synthase
Enzyme E.C.: 7.1.2.2
Where the enzyme is located? ATP synthase is located transcending across energy transducing membranes such as the inner mitochondrial membrane, thylakoid membranes and plasma membranes of eubacteria and archaebacteria. ATP synthase is composed of two subunits, F0 and F1 with the F0 subunit embedded in the membrane and the F1 subunit outside of the membrane facing the side with low proton concentration. In the mitochondria, the F0 subunit is embedded in the inner mitochondrial membrane while the F1 subunit is in the mitochondrial matrix.
What the enzyme does – ATP synthase synthesizes adenosine triphosphate from adenosine diphosphate and inorganic phosphate. This is an endothermic reaction and requires the addition of energy. ATP synthase does this by coupling the reaction to the movement of protons from high concentration to low concentration in an electrochemical proton gradient.
Other interesting facts and important information about the enzyme – This enzyme uses metal ion catalysis, using a magnesium ion to neutralize charges that cause repulsion. This lowers the activation energy and allows for the reaction to proceed. The enzyme contains six active sites, three of which are active and three are inactive. The active sites are made up of a specific amino acid sequence known as the “p-loop.” Each active site changes its conformation from the rotation of the F1 component to interact differently with the substrate.
References:
Ahmad, Z., Okafor, F., & Laughlin, T. F. (2011). Role of Charged Residues in the Catalytic Sites ofEscherichia coliATP Synthase. Journal of Amino Acids, 2011, 1–12. https://doi.org/10.4061/2011/785741
Alberts, B., Johnson, A., Lewis, J., Raff, M., Roberts, K., & Walter, P. (2013). The Mitochondrion. Nih.gov; Garland Science. https://www.ncbi.nlm.nih.gov/books/NBK26894/
Blum, D. J., Ko, Y. H., & Pedersen, P. L. (2012). Mitochondrial ATP Synthase Catalytic Mechanism: A Novel Visual Comparative Structural Approach Emphasizes Pivotal Roles for Mg2+ and P-Loop Residues in Making ATP. Biochemistry, 51(7), 1532–1546. https://doi.org/10.1021/bi201595v
Boyer, P. D. (2002). Catalytic site occupancy during ATP synthase catalysis. FEBS Letters, 512(1-3), 29–32. https://doi.org/10.1016/s0014-5793(02)02293-7
David L Nelson, Micheal M. Cox. (2017). Leininger Principles of Biochemistry. Seventh Edition. Macmillan Learning.
EC 7.1.2.2. (n.d.). Iubmb.qmul.ac.uk. https://iubmb.qmul.ac.uk/enzyme/EC7/1/2/2.html
Harvard Online. (2017, April 19). ATP Synthase in Action [Video]. Youtube. https://youtu.be/kXpzp4RDGJI?si=eTluZ0wUdRk7NWGS
Yeagle, P. L. (2016, January 1). Chapter 13 – Membrane Transport (P. L. Yeagle, Ed.). ScienceDirect; Academic Press. https://www.sciencedirect.com/science/article/abs/pii/B9780128000472000139
